GenomeNet

Database: UniProt
Entry: A0A252BMJ0_9PROT
LinkDB: A0A252BMJ0_9PROT
Original site: A0A252BMJ0_9PROT 
ID   A0A252BMJ0_9PROT        Unreviewed;       770 AA.
AC   A0A252BMJ0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:OUJ08049.1};
GN   Name=clpA {ECO:0000313|EMBL:OUJ08049.1};
GN   ORFNames=HK24_03530 {ECO:0000313|EMBL:OUJ08049.1};
OS   Gluconobacter sp. DsW_058.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=1511210 {ECO:0000313|EMBL:OUJ08049.1, ECO:0000313|Proteomes:UP000194786};
RN   [1] {ECO:0000313|Proteomes:UP000194786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Winans N.J., Newell P.D., Douglas A.E.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUJ08049.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JOPH01000033; OUJ08049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A252BMJ0; -.
DR   Proteomes; UP000194786; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043335; P:protein unfolding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR013461; ClpA.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02639; ClpA; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Hydrolase {ECO:0000313|EMBL:OUJ08049.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OUJ08049.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194786};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          148..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  85014 MW;  6040A58278DE018E CRC64;
     MLSRTLEQTL HRALTFAGDR RHEYATLEHL LLALTEDADA LTVFRACGID LDKLRSDLTD
     FLDKDLAGLA SDRPTEPKPT AAFQRVIQRA AIHVQSTGRD EVTGANVLVA LFAERESHAV
     YFLQLQDMTR LDAVNFISHG IAKAPDRGAG RKAAAASKDN SEREERKETA KDGALATYCV
     NLNDRAREGR IDPLIGRDQE IERTIQILCR RTKNNPLYVG DPGVGKTAIA EGLAKRIVEK
     DVPEVLQDCT IYSLDMGSLL AGTRYRGDFE ERLKAVVTEM DQTPGAILFI DEIHTVIGAG
     ATSGGAMDAS NLLKPALAAG TLRCIGSTTY KEFRQHFEKD RALVRRFQKI DVPEPSVEDT
     IKILRGLKGS YEKHHKVRYT DEALRGAVEL AARYVHDRKL PDKAIDVIDE VGAARMLVPE
     NKRRKTVTLR DVEDAIAKIA RIPPKSVTAD DRETLRHLER DLRNMVFGQD KAIDALAAAI
     KLSRAGLRDA EKPIGNYLFS GPTGVGKTEV ARQLASSLGI ELIRFDMSEY MERHSISRLI
     GAPPGYVGFD QGGLLTDAID QHPHAVLLLD EIEKAHPDLY NVLLQVMDHG RLTDHNGKTV
     DFRNVILIMT TNAGAADLSK EAIGFGRTSR AGEDEEAIKR TFTPEFRNRL DAIIPFANLT
     PETVGRVVEK FVLQLEAQLA DRHVTIEISS AAKEWLAEKG YDRLYGARPL GRVIQEHIKK
     PLAEELLFGR LAKGGAVKIG LKNDVLDFEI IEGTGVKGDS SAEKKDEAAN
//
DBGET integrated database retrieval system